Research Article
Year 2018,
Volume: 39 Issue: 4, 828 - 832, 24.12.2018
Abstract
The vast majority of the carbohydrates in the biomolecule class are
formed by photosynthesis using sunlight. One of the important enzymes in this
class is α-glycosidase. This enzyme converts complex carbohydrates to
monosaccharides. On the other hand, another important enzyme species is the
α-amylase enzyme. Which directly related to starch. Starch is a type of polymer
formed by the oxygen binding of glucose units to each other at the C1 position
with glycosidic bonds. α-Amylase is an enzyme that catalyzes the hydrolysis of
glycosidic bonds in starch, and this enzyme is purified from a wide variety of
animals, plants, and microorganisms. Resorcinol, a phenol derivative, is an
important organic chemical substance in the production of textile, medicine,
hair dye, plastic and agricultural products of many industrial materials.
Resorcinol, a phenol derivative, is present as white crystals, and resorcinol
consists of two hydroxyl molecules attached to the benzene ring, and also was
defined as α-glycosidase and α-amylase inhibitor to detect antidiabetic
properties. Resorcinol was used as 𝛼-glycosidase and 𝛼-amylase inhibitor. Accordingly, IC50 values of α-amylase and
α-glycosidase were calculated as 1.34 μM and 77.00 nM, respectively. On the
other hand, Ki value for α-glycosidase was found as 30.16 nM. It has
been observed that α-amylase and α-glycosidase enzymes can inhibit by
resorcinol compound. It has the properties of inhibiting carbohydrate
absorption by inhibiting α-glycosidase enzymes in the small intestine. For both metabolic
enzymes, resorcinol may be preferred as an inhibitor. In this case, resorcinol
may be used as an inhibitor against to healty problems like Diabetes
mellitus and antiobesity.
formed by photosynthesis using sunlight. One of the important enzymes in this
class is α-glycosidase. This enzyme converts complex carbohydrates to
monosaccharides. On the other hand, another important enzyme species is the
α-amylase enzyme. Which directly related to starch. Starch is a type of polymer
formed by the oxygen binding of glucose units to each other at the C1 position
with glycosidic bonds. α-Amylase is an enzyme that catalyzes the hydrolysis of
glycosidic bonds in starch, and this enzyme is purified from a wide variety of
animals, plants, and microorganisms. Resorcinol, a phenol derivative, is an
important organic chemical substance in the production of textile, medicine,
hair dye, plastic and agricultural products of many industrial materials.
Resorcinol, a phenol derivative, is present as white crystals, and resorcinol
consists of two hydroxyl molecules attached to the benzene ring, and also was
defined as α-glycosidase and α-amylase inhibitor to detect antidiabetic
properties. Resorcinol was used as 𝛼-glycosidase and 𝛼-amylase inhibitor. Accordingly, IC50 values of α-amylase and
α-glycosidase were calculated as 1.34 μM and 77.00 nM, respectively. On the
other hand, Ki value for α-glycosidase was found as 30.16 nM. It has
been observed that α-amylase and α-glycosidase enzymes can inhibit by
resorcinol compound. It has the properties of inhibiting carbohydrate
absorption by inhibiting α-glycosidase enzymes in the small intestine. For both metabolic
enzymes, resorcinol may be preferred as an inhibitor. In this case, resorcinol
may be used as an inhibitor against to healty problems like Diabetes
mellitus and antiobesity.
References
- [1]. Taslimi P. and Gulcin I., Antidiabetic potential: in vitro inhibition effects of some natural phenolic compounds on α-glycosidase and α-amylase enzymes, Journal of Biochemical and Molecular Toxicology, 31(2017), e21956.
- [2]. Cengiz Ecemis G. and Atmaca H., Oral antidiabetic agents, Journal of Experimental and Clinical Medicine, 29(2012), 23-29.
- [3]. Tuzlakoglu Ozturk M., Yerel bacillus İzolatlarından alfa Amilazların Klonlanması ve Rekombinant amy28 alfa Amilazının Enzim Özelliklerinin Belirlenmesi, Gebze Yüksek Teknoloji Enstitüsü Mühendislik ve Fen Bilimleri Enstitüsü, Doktora Tezi, Gebze (2013).
- [4]. Oztolan O., Alfa Amilaz-Dekstran Konjugatlarının Sentezi Ve Karakterizasyonu, Yıldız Teknik Üniversitesi Fen Bilimleri Enstitüsü, Yüksek Lisans Tezi, İstanbul (2007).
- [5]. Xiao, Z., Storms, R. and Tsang, A., A quantitative starch-iodine method for measuring alpha-amylase and glucoamylase activities. Analytical Biochemistry, 351(2006), 146-148.
- [6]. Taslimi P., Akıncıoğlu H. and Gulcin I., Synephrine and phenylephrine act as α-amylase, α-glycosidase, acetylcholinesterase, butyrylcholinesterase and carbonic anhydrase enzymes inhibitors. Journal of Biochemical and Molecular Toxicology, 31(2017), 11, e21973.
- [7]. Uysal A., Zengin G., Durak Y. and Aktumsek A., Centaurea pterocaula özütlerinin antioksidan ve antimutajenik özellikleri ile enzim inhibitör potansiyellerinin incelenmesi. Marmara Pharmaceutical Journal, 20(2016), 232-242.
- [8]. Enache TA. and Oliveira-Brett AM., Phenol and parasubstituted phenols electrochemical oxidation pathways, Journal of Electroanalytical Chemistry, 655(2011), 9-16.
- [9]. Salazar R., Vidal J., Martínez-Cifuentes M., Araya-Maturana R. and Ramírez-Rodríguez O., Electrochemical characterization of hydroquinone derivatives with different substituents in acetonitrile, New Journal of Chemistry, 39(2015), 1237-1246.
- [10]. Dunlap T,, Chandrasena REP., Wang Z., Sinha V., Wang Z. and Thatcher GRJ., Quinone Formation as a Chemoprevention Strategy for Hybrid Drugs: Balancing Cytotoxicity and Cytoprotection, Chemical Research Toxicology, 20(2007), 1903-1912.
- [11]. Zhang Z., Yuan Lian X., Li S.and Stringer JL., Characterization of chemical ingredients and anticonvulsant activity of American skullcap (Scutellaria lateriflora), Phytomedicine, 16(2009), 485-493.
- [12]. Tao Y., Zhang Y., Cheng Y. and Wang Y., Rapid screening and identification of α-glucosidase inhibitors from mulberry leaves using enzyme-immobilized magnetic beads coupled with HPLC/MS and NMR, Biomedical Chromatography, 27(2013), 148-155.
- [13]. Xiao Z., Storms R. and Tsang A., A quantitative starch-iodine method for measuring alpha-amylase and glucoamylase activities, Analytical Biochemistry, 351(2006), 146-8.
- [14]. Varan G., Yeni Tanı Almış Prediyabetik ve Diyabetik Hastalarda Akarboz Kullanımının Metabolik Parametreler Üzerine Etkisi, Mustafa Kemal Üniversitesi Tayfur Ata Sökmen Tıp Fakültesi, Uzmanlık Tezi, Hatay (2015).
- [15]. Teng H., Chen L., Fang T., Yuan B. and Lin Q., Rb2 inhibits a-glucosidase and regulates glucose metabolism by activating AMPK pathways in HepG2 cells, Journal of Functional Foods, 28(2017), 306-313.
- [16]. Torres-Naranjo M., Suárez A., Gilardoni G., Cartuche L., Flores P. and Morocho V., Chemical Constituents of Muehlenbeckia tamnifolia (Kunth) Meisn (Polygonaceae) and Its In Vitro α-Amilase and α-Glucosidase Inhibitory Activities, Molecules, 21(2016), 1461.
Year 2018,
Volume: 39 Issue: 4, 828 - 832, 24.12.2018
Abstract
Biyomolekül sınıfında bulunan karbohidratların büyük çoğunluğu güneş
ışığını kullanarak fotosentez sonucu oluşurlar. Bu sınıfın önemli enzimlerinden
birisi ise 𝛼-Glikozidaz dır. Bu
enzim, kompleks karbohidratları monosakkaritlere dönüştürür. Diğer taraftan bir
başka önemli enzim türü ise α-amilaz
enzimidir. Bu enzim ise nişasta ile doğrudan ilişkilidir. Nişasta,
glukoz ünitelerinin birbirine glikozidik bağlarla C1 pozisyonunda yer alan
oksijenden bağlanmasıyla oluşan bir polimer türüdür. α-Amilaz, nişastada bulunan bu glikozidik bağların hidrolizini
katalizleyen enzimlerdir ve bu enzim çok çeşitli hayvan, bitki ve
mikroorganizmalardan saflaştırılmaktadır. Bir fenol türevi olan resorsinol,
birçok endüstriyel malzemelerin tekstil, ilaç, saç boyaları, plastik ve tarım
ürünlerinin üretiminde önemli bir organik kimyasal maddedir. Fenol türevi olan
resorsinol beyaz kristaller halinde bulunur ve resorsinol benzen halkasına
bağlı iki hidroksil molekülünden oluşur. 𝛼-Glikozidaz ve 𝛼-amilaz inhibitörü olarak resorsinol kullanıldı. Buna göre α-amilaz ve
α-glikosidaz, sırasıyla IC50 değerleri 1,34 µM ve 77,00 nM olarak
hesaplandı. Öte yandan, α-glikosidaz için Ki değeri 30,16 nM olarak
bulundu. 𝛼-Amilaz ve 𝛼-glikozidaz enzimlerini resorsinol bileşiği inhibe edebildiği
gözlemlendi. İnce barsakta 𝛼-glukozidaz enzimlerini
inhibe ederek karbohidrat emilimini geciktirme özelliklerine sahiptirler. Her
iki metabolik enzim için resorsinol, bir inhibitör olarak tercih edilebilir. Bu
durumda resorsinol, Diyabet
mellitus ve antiobezite gibi sağlık sorunlarına karşı inhibitör olarak
kullanılabilir.
References
- [1]. Taslimi P. and Gulcin I., Antidiabetic potential: in vitro inhibition effects of some natural phenolic compounds on α-glycosidase and α-amylase enzymes, Journal of Biochemical and Molecular Toxicology, 31(2017), e21956.
- [2]. Cengiz Ecemis G. and Atmaca H., Oral antidiabetic agents, Journal of Experimental and Clinical Medicine, 29(2012), 23-29.
- [3]. Tuzlakoglu Ozturk M., Yerel bacillus İzolatlarından alfa Amilazların Klonlanması ve Rekombinant amy28 alfa Amilazının Enzim Özelliklerinin Belirlenmesi, Gebze Yüksek Teknoloji Enstitüsü Mühendislik ve Fen Bilimleri Enstitüsü, Doktora Tezi, Gebze (2013).
- [4]. Oztolan O., Alfa Amilaz-Dekstran Konjugatlarının Sentezi Ve Karakterizasyonu, Yıldız Teknik Üniversitesi Fen Bilimleri Enstitüsü, Yüksek Lisans Tezi, İstanbul (2007).
- [5]. Xiao, Z., Storms, R. and Tsang, A., A quantitative starch-iodine method for measuring alpha-amylase and glucoamylase activities. Analytical Biochemistry, 351(2006), 146-148.
- [6]. Taslimi P., Akıncıoğlu H. and Gulcin I., Synephrine and phenylephrine act as α-amylase, α-glycosidase, acetylcholinesterase, butyrylcholinesterase and carbonic anhydrase enzymes inhibitors. Journal of Biochemical and Molecular Toxicology, 31(2017), 11, e21973.
- [7]. Uysal A., Zengin G., Durak Y. and Aktumsek A., Centaurea pterocaula özütlerinin antioksidan ve antimutajenik özellikleri ile enzim inhibitör potansiyellerinin incelenmesi. Marmara Pharmaceutical Journal, 20(2016), 232-242.
- [8]. Enache TA. and Oliveira-Brett AM., Phenol and parasubstituted phenols electrochemical oxidation pathways, Journal of Electroanalytical Chemistry, 655(2011), 9-16.
- [9]. Salazar R., Vidal J., Martínez-Cifuentes M., Araya-Maturana R. and Ramírez-Rodríguez O., Electrochemical characterization of hydroquinone derivatives with different substituents in acetonitrile, New Journal of Chemistry, 39(2015), 1237-1246.
- [10]. Dunlap T,, Chandrasena REP., Wang Z., Sinha V., Wang Z. and Thatcher GRJ., Quinone Formation as a Chemoprevention Strategy for Hybrid Drugs: Balancing Cytotoxicity and Cytoprotection, Chemical Research Toxicology, 20(2007), 1903-1912.
- [11]. Zhang Z., Yuan Lian X., Li S.and Stringer JL., Characterization of chemical ingredients and anticonvulsant activity of American skullcap (Scutellaria lateriflora), Phytomedicine, 16(2009), 485-493.
- [12]. Tao Y., Zhang Y., Cheng Y. and Wang Y., Rapid screening and identification of α-glucosidase inhibitors from mulberry leaves using enzyme-immobilized magnetic beads coupled with HPLC/MS and NMR, Biomedical Chromatography, 27(2013), 148-155.
- [13]. Xiao Z., Storms R. and Tsang A., A quantitative starch-iodine method for measuring alpha-amylase and glucoamylase activities, Analytical Biochemistry, 351(2006), 146-8.
- [14]. Varan G., Yeni Tanı Almış Prediyabetik ve Diyabetik Hastalarda Akarboz Kullanımının Metabolik Parametreler Üzerine Etkisi, Mustafa Kemal Üniversitesi Tayfur Ata Sökmen Tıp Fakültesi, Uzmanlık Tezi, Hatay (2015).
- [15]. Teng H., Chen L., Fang T., Yuan B. and Lin Q., Rb2 inhibits a-glucosidase and regulates glucose metabolism by activating AMPK pathways in HepG2 cells, Journal of Functional Foods, 28(2017), 306-313.
- [16]. Torres-Naranjo M., Suárez A., Gilardoni G., Cartuche L., Flores P. and Morocho V., Chemical Constituents of Muehlenbeckia tamnifolia (Kunth) Meisn (Polygonaceae) and Its In Vitro α-Amilase and α-Glucosidase Inhibitory Activities, Molecules, 21(2016), 1461.
There are 16 citations in total.
Details
| Primary Language | English |
|---|---|
| Journal Section | Natural Sciences |
| Authors | |
| Publication Date | December 24, 2018 |
| Submission Date | August 9, 2018 |
| Acceptance Date | November 2, 2018 |
| Published in Issue | Year 2018Volume: 39 Issue: 4 |